The dynamic disulphide relay of quiescin sulphydryl oxidase
Assaf Alon,
Iris Grossman,
Yair Gat,
Vamsi K. Kodali,
Frank DiMaio,
Tevie Mehlman,
Gilad Haran,
David Baker,
Colin Thorpe and
Deborah Fass ()
Additional contact information
Assaf Alon: Weizmann Institute of Science, Rehovot 76100, Israel
Iris Grossman: Weizmann Institute of Science, Rehovot 76100, Israel
Yair Gat: Weizmann Institute of Science, Rehovot 76100, Israel
Vamsi K. Kodali: University of Delaware
Frank DiMaio: University of Washington
Tevie Mehlman: Weizmann Institute of Science, Rehovot 76100, Israel
Gilad Haran: Weizmann Institute of Science, Rehovot 76100, Israel
David Baker: University of Washington
Colin Thorpe: University of Delaware
Deborah Fass: Weizmann Institute of Science, Rehovot 76100, Israel
Nature, 2012, vol. 488, issue 7411, 414-418
Abstract:
The X-ray crystal structures of trypanosome and mammalian quiescin sulphydryl oxidase are determined; these structures and follow-up biochemical studies show that large conformational changes occur as the enzyme relays disulphide bonds through its redox-active sites.
Date: 2012
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DOI: 10.1038/nature11267
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